ID   PTPA_STAAC              Reviewed;         154 AA.
AC   Q5HEP3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Low molecular weight protein-tyrosine-phosphatase PtpA;
DE            EC=3.1.3.48;
DE   AltName: Full=Phosphotyrosine phosphatase A;
DE            Short=PTPase A;
GN   Name=ptpA; OrderedLocusNames=SACOL1939;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
CC   -!- FUNCTION: Secreted tyrosine phosphatase that plays a critical role
CC       during infection as a bacterial effector protein that counteracts host
CC       defenses. Required for intramacrophage survival.
CC       {ECO:0000250|UniProtKB:A0A0H3K9F2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620; EC=3.1.3.48;
CC         Evidence={ECO:0000250|UniProtKB:A0A0H3K9F2};
CC   -!- SUBUNIT: Interacts with host CORO1A.
CC       {ECO:0000250|UniProtKB:A0A0H3K9F2}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:A0A0H3K9F2}.
CC       Note=Secreted intracellularly upon bacterial infection of macrophages.
CC       {ECO:0000250|UniProtKB:A0A0H3K9F2}.
CC   -!- PTM: Phosophorylations at Tyr-122 and Tyr-123 are essential for
CC       phosphatase activity. {ECO:0000250|UniProtKB:A0A0H3K9F2}.
CC   -!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein
CC       phosphatase family. {ECO:0000305}.
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DR   EMBL; CP000046; AAW38380.1; -; Genomic_DNA.
DR   RefSeq; WP_000228666.1; NC_002951.2.
DR   AlphaFoldDB; Q5HEP3; -.
DR   SMR; Q5HEP3; -.
DR   EnsemblBacteria; AAW38380; AAW38380; SACOL1939.
DR   KEGG; sac:SACOL1939; -.
DR   HOGENOM; CLU_071415_2_3_9; -.
DR   OMA; TGSWHVG; -.
DR   Proteomes; UP000000530; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   InterPro; IPR023485; Ptyr_pPase.
DR   InterPro; IPR036196; Ptyr_pPase_sf.
DR   InterPro; IPR017867; Tyr_phospatase_low_mol_wt.
DR   Pfam; PF01451; LMWPc; 1.
DR   PRINTS; PR00719; LMWPTPASE.
DR   SMART; SM00226; LMWPc; 1.
DR   SUPFAM; SSF52788; SSF52788; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Phosphoprotein; Protein phosphatase; Secreted.
FT   CHAIN           1..154
FT                   /note="Low molecular weight protein-tyrosine-phosphatase
FT                   PtpA"
FT                   /id="PRO_0000300658"
FT   ACT_SITE        8
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
FT   ACT_SITE        14
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
FT   ACT_SITE        120
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
SQ   SEQUENCE   154 AA;  17491 MW;  67E81E0B8125B1E8 CRC64;
     MVDVAFVCLG NICRSPMAEA IMRQRLKDRN IHDIKVHSRG TGSWNLGEPP HEGTQKILNK
     HNIPFDGMIS ELFEATDDFD YIVAMDQSNV DNIKSINPNL KGQLFKLLEF SNMEESDVPD
     PYYTNNFEGV YDMVLSSCDN LIDYIVKDAN LKEG